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SUMOylation regulates AKT1 activity

Cruz-Herrera, C.F.; Campagna M; Lang V; del Carmen González-Santamaría, J; Marcos-Villar, L; Rodríguez, MS; Vidal Figueroa, Anxo; Collado Rodríguez, Manuel; Rivas, C
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URI: http://hdl.handle.net/20.500.11940/8180
PMID: 24704831
DOI: 10.1038/onc.2014.48
ISSN: 0950-9232
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Texto completo disponible por cortesía de Oncogene . 2015 Mar 12;34(11):1442-50 (1.529Mb)
Fecha de publicación
2015
Título de revista
ONCOGENE
Tipo de contenido
Artigo
MeSH
3T3 Cells | Animals | Apoptosis | COS Cells | Cell Line, Tumor | Cell Proliferation | Chlorocebus aethiops | Enzyme Activation | Female | HEK293 Cells | HeLa Cells | Humans | MCF-7 Cells | Mice | Mutation | Neoplasms | Phosphoinositide-3 Kinase Inhibitors | Phosphorylation | Proto-Oncogene Proteins c-akt | SUMO-1 Protein | Small Ubiquitin-Related Modifier Proteism | Sumoylatigy | Ubiquitism
Resumen
Serine threonine kinase AKT has a central role in the cell, controlling survival, proliferation, metabolism and angiogenesis. Deregulation of its activity underlies a wide range of pathological situations, including cancer. Here we show that AKT is post-translationally modified by the small ubiquitin-like modifier (SUMO) protein. Interestingly, neither SUMO conjugation nor activation of SUMOylated AKT is regulated by the classical AKT targeting to the cell membrane or by the phosphoinositide 3-kinase pathway. We demonstrate that SUMO induces the activation of AKT, whereas, conversely, down-modulation of the SUMO machinery diminishes AKT activation and cell proliferation. Furthermore, an AKT SUMOylation mutant shows reduced activation, and decreased anti-apoptotic and pro-tumoral activities in comparison with the wild-type protein. These results identify SUMO as a novel key regulator of AKT phosphorylation and activity.

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